The pathway, in which a protein folds, is most likely governed by early "seeding" events and transient conformational changes defined by the biomolecules primary sequence. In order to understand fully the correlation between the primary sequence and the pathway through which proteins fold to their native conformations will require knowledge of the entire kinetic history. Current stopped flow methods can following the folding events over a range from milliseconds and longer, yet, there is significant information lost in the stopped-flow dead time (less than milliseconds in time). We have synthesized several alpha helical peptides which are stabilized by a disulfide bridge. Using picosecond and nanosecond transient absorption techniques, we have triggered peptide unfolding reactions and have followed the kinetics of unfolding on a time scale several orders in magnitude faster than observed using current methods.